Recent insights into cysteine protease specificity: Lessons for drug design

1996 ◽  
Vol 6 (1) ◽  
pp. 33-46 ◽  
Author(s):  
Andrew C. Storer ◽  
Robert Ménard
Keyword(s):  
Drug Design ◽  
Cysteine Protease ◽  
Protease Specificity

scholarly journals Boophilus microplus cathepsin L-like (BmCL1) cysteine protease: Specificity study using a peptide phage display library

2011 ◽  
Vol 181 (2-4) ◽  
pp. 291-300 ◽  
Author(s):  
Renan O. Clara ◽  
Tatiane S. Soares ◽  
Ricardo J.S. Torquato ◽  
Cássia A. Lima ◽  
Renata O.M. Watanabe ◽  
...  
Keyword(s):  
Phage Display ◽  
Cysteine Protease ◽  
Cathepsin L ◽  
Phage Display Library ◽  
Boophilus Microplus ◽  
Peptide Phage Display ◽  
Specificity Study ◽  
Protease Specificity

scholarly journals Cruzain structures: apocruzain and cruzain bound to S-methyl thiomethanesulfonate and implications for drug design

2019 ◽  
Vol 75 (6) ◽  
pp. 419-427 ◽  
Author(s):  
Elany Barbosa da Silva ◽  
Elfriede Dall ◽  
Peter Briza ◽  
Hans Brandstetter ◽  
Rafaela Salgado Ferreira
Keyword(s):  
Drug Design ◽  
Trypanosoma Cruzi ◽  
Chagas Disease ◽  
Cysteine Protease ◽  
In Silico ◽  
Structural Information ◽  
Mass Spectrometric ◽  
Catalytic Cysteine ◽  
Reversible Covalent ◽  
Covalent Inhibitor

Chagas disease, which is caused by Trypanosoma cruzi, affects more than six million people worldwide. Cruzain is the major cysteine protease involved in the survival of this parasite. Here, the expression, purification and crystallization of this enzyme are reported. The cruzain crystals diffracted to 1.2 Å resolution, yielding two novel cruzain structures: apocruzain and cruzain bound to the reversible covalent inhibitor S-methyl thiomethanesulfonate. Mass-spectrometric experiments confirmed the presence of a methylthiol group attached to the catalytic cysteine. Comparison of these structures with previously published structures indicates the rigidity of the cruzain structure. These results provide further structural information about the enzyme and may help in new in silico studies to identify or optimize novel prototypes of cruzain inhibitors.

The cysteine protease of Trypanosoma cruzi as a model for antiparasite drug design

1995 ◽  
Vol 11 (8) ◽  
pp. 279-282 ◽  
Author(s):  
J.H. McKerrow ◽  
M.E. McGrath ◽  
J.C. Engel
Keyword(s):  
Drug Design ◽  
Trypanosoma Cruzi ◽  
Cysteine Protease

Multi-targeted design and development of dihydroisoquinolines as potent antimalarial

2019 ◽  
Vol 15 ◽  
Author(s):  
Raviraj V. Mule ◽  
Sneha P. Rochlani ◽  
Prafulla B. Choudhari ◽  
Rakesh P Dhavale ◽  
Manish S. Bhatia
Keyword(s):  
Multidrug Resistance ◽  
Drug Design ◽  
Cysteine Protease ◽  
Antimalarial Activity ◽  
Docking Study ◽  
Hydrogen Binding ◽  
Design And Development ◽  
Binding Interaction ◽  
Structure Based Drug Design ◽  
Antimalarial Agents

Background: Cysteine protease and DHODH enzyme were identified as potential target and for synthesized compound which revealed binding interaction and confirmation from docking study. Development of new lead which specifically targeting cysteine protease and DHODH enzyme can be able to reduce the side effect and to overcome multidrug resistance. Objectives: Design and development of antimalarial agents by targeting cysteine protease and DHODH (Dihydroorotate dehydrogenase) enzyme by structure based drug design. Materials and Methods: In present work, rational development of antimalarial agents by targeting cysteine protease and DHODH has been done by integrating binding confirmation from virtual analysis and synthetic procedures. Result: A novel series of dihydroisoquinolines were designed by structure based drug design. Large compounds of dataset were screened for molecular docking study and subsequently all molecules were screened for drug like properties and toxicity study prior to synthesis. The designed molecules which analysed by virtual screening were synthesized, characterized and finally screened for antimalarial activity by performing bioassay. Synthesized compounds were showed greater antimalarial activity in terms percent inhibition. Conclusion: In this work, compound A1,A5,A6,A9 showed desirable inhibitory activity toward targets in terms of percentage and also specific hydrogen binding interaction with those targets. Further optimization in leads able to yield drug like candidate and it may able to overcome multidrug resistance.

Immunohistochemical localization of lysosomal cysteine protease cathepsins B and L in monkey hippocampal neurons after transient ischemia

1999 ◽  
Vol 19 (3) ◽  
pp. 302-310
Author(s):  
Yukihiko Kohda ◽  
Katsuhiro Tsuchiya ◽  
Junkoh Yamashita ◽  
Masaki Yoshida ◽  
Takashi Ueno ◽  
...  
Keyword(s):  
Cysteine Protease ◽  
Hippocampal Neurons ◽  
Immunohistochemical Localization ◽  
Transient Ischemia ◽  
Lysosomal Cysteine Protease
Sign in / Sign up

Export Citation Format

Share Document